node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AQS55143.1 | AQS55145.1 | B0W44_04525 | B0W44_04535 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AQS55143.1 | AQS55173.1 | B0W44_04525 | B0W44_04690 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
AQS55143.1 | AQS56691.1 | B0W44_04525 | B0W44_13945 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
AQS55143.1 | AQS56723.1 | B0W44_04525 | B0W44_14165 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.998 |
AQS55143.1 | AQS56724.1 | B0W44_04525 | B0W44_14170 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AQS55143.1 | AQS56829.1 | B0W44_04525 | B0W44_14810 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.984 |
AQS55143.1 | AQS56830.1 | B0W44_04525 | B0W44_14815 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.984 |
AQS55143.1 | AQS57082.1 | B0W44_04525 | B0W44_16320 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.995 |
AQS55143.1 | AQS57584.1 | B0W44_04525 | B0W44_14160 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AQS55143.1 | nuoD | B0W44_04525 | B0W44_16975 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.965 |
AQS55145.1 | AQS55143.1 | B0W44_04535 | B0W44_04525 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.999 |
AQS55145.1 | AQS55173.1 | B0W44_04535 | B0W44_04690 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.833 |
AQS55145.1 | AQS56691.1 | B0W44_04535 | B0W44_13945 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.922 |
AQS55145.1 | AQS56723.1 | B0W44_04535 | B0W44_14165 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.964 |
AQS55145.1 | AQS56724.1 | B0W44_04535 | B0W44_14170 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
AQS55145.1 | AQS56829.1 | B0W44_04535 | B0W44_14810 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.774 |
AQS55145.1 | AQS56830.1 | B0W44_04535 | B0W44_14815 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Peptidase M16; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.774 |
AQS55145.1 | AQS57082.1 | B0W44_04535 | B0W44_16320 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.925 |
AQS55145.1 | AQS57584.1 | B0W44_04535 | B0W44_14160 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.984 |
AQS55145.1 | nuoD | B0W44_04535 | B0W44_16975 | Cytochrome (ubi)quinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.824 |